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NADP(H)-dependent biocatalysis without adding NADP(H).

Ryan A Herold1, Raphael Reinbold2, Christopher J Schofield2

  • 1Department of Chemistry, University of Oxford, Oxford OX1 3QR, United Kingdom.

Proceedings of the National Academy of Sciences of the United States of America
|December 27, 2022
PubMed
Summary
This summary is machine-generated.

Nanoconfinement dramatically boosts enzyme efficiency by entrapping cofactors, enabling sustained catalysis for days. This electrochemical approach enhances redox cycling and reveals cofactor binding differences in enzyme variants.

Keywords:
NADPHbiocatalysiselectrocatalysisisocitrate dehydrogenasenanoconfinement

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Area of Science:

  • Biochemistry
  • Electrochemistry
  • Nanotechnology

Background:

  • Isocitrate dehydrogenase 1 (IDH1) naturally binds its cofactor NADP+/NADPH.
  • Multistep enzyme cascade reactions often suffer from low efficiency.

Purpose of the Study:

  • To investigate the impact of nanoconfinement on enzyme-catalyzed cascade reactions.
  • To explore the use of entrapped cofactors for sustained enzymatic activity.
  • To study cofactor binding differences between wild-type and variant IDH1.

Main Methods:

  • Electrochemical studies using IDH1 and ferredoxin NADP+ reductase.
  • Loading enzymes and cofactors into nanoporous indium tin oxide films.
  • Cyclic voltammetry to quantify cofactor turnovers.
  • Electrocatalysis experiments to drive reactions in both directions.

Main Results:

  • Nanoconfinement increased NADP(H) redox cycling efficiency by 10^2 to 10^3-fold.
  • The system remained active for days, with entrapped cofactors undergoing ~160,000 turnovers.
  • Identified differences in cofactor binding between wild-type IDH1 and the R132H variant.

Conclusions:

  • Nanoconfinement is a powerful strategy for enhancing multistep enzyme catalysis.
  • Entrapped cofactors facilitate sustained and efficient redox cycling.
  • The study provides insights into the role of nicotinamide cofactors in redox reactions and enzyme variants.